Cloned (Comment) | Organism |
---|---|
recombinant expression of HA-tagged wild-type and K82M mutant enzymes in Spodoptera frugiperda Sf9 cells | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K82M | a kinase-inactive mutant | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
kinetochore | - |
Homo sapiens | 776 | - |
nucleus | - |
Homo sapiens | 5634 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + CENP-Q | Homo sapiens | - |
ADP + phosphorylated CENP-Q | - |
? | |
ATP + PBIP1 | Homo sapiens | Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism | ADP + phosphorylated PBIP1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9NYY3 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant HA-tagged wild-type and K82M mutant enzymes from Spodoptera frugiperda Sf9 cells | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HeLa cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + CENP-Q | - |
Homo sapiens | ADP + phosphorylated CENP-Q | - |
? | |
ATP + CENP-Q | phosphorylation of nine CENP-Q residues Thr123, Thr135, Ser138, Ser139, Ser248, Ser249, Ser253, Ser255, and Thr256, clustered in two regions, mutation of all nine residues to Ala completely eliminated Plk1-dependent CENP-Q phosphorylation in vitro | Homo sapiens | ADP + phosphorylated CENP-Q | - |
? | |
ATP + PBIP1 | Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism | Homo sapiens | ADP + phosphorylated PBIP1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Plk1 | - |
Homo sapiens |
Polo-like kinase 1 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | a failure in Plk1 regulation of the timing of CENP-Q dissociation from kinetochores leads to chromosome missegregation. Inhibition of Plk1 activity greatly diminishes hyperphosphorylates, slow-migrating PBIP1 (but not the moderately phosphorylated PBIP1 forms because of the presence of Plk1-independent phosphorylation) and appears to eliminate slow-migrating CENP-Q forms | Homo sapiens |
metabolism | cell cycle-dependent regulation of the PBIP1-CENP-Q complex involving the enzyme, overview | Homo sapiens |
physiological function | Plk1 is a protein kinase that localizes to subcellular structures called kinetochores to promote mitotic progression. Plk1 interacts with and regulates a kinetochore-associated PBIP1-CENP-Q complex. This is a tightly regulated, cell cycle-dependent process, the deregulation of which leads to improper chromosome segregation and mitotic progression. The event is likely critical for maintaining genomic integrity and preventing aneuploidy. PBIP1 and CENP-Q are ubiquitinated in a manner that does not require Plk1. Plk1 dissociates CENP-Q from chromatin without disrupting the PBIP1-CENP-Q complex. Plk1-dependent CENP-Q phosphorylation negatively regulates the ability of the PBIP1-CENP-Q complex to associate with chromatin. Plk1 regulates the timing of CENP-Q dissociation from kinetochores. Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism and then phosphorylates the CENP-Q subunit of the PBIP1-CENP-Q complex | Homo sapiens |